Protein profile

PA1546

oxygen-independent coproporphyrinogen-III oxidase

Genome: NC_002516.2

Gene: hemN PA1546 Structure source: AlphaFold UniProt P77915
Amino acids 460
Annotations 10
Features 24
PDB binders 0
Druggability 0.823

Overview

Basic information about this protein and its source genome.

Accession
PA1546
Gene
hemN PA1546
Status
annotated
Amino acids
460
Structure source
AlphaFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
30.645
Human E-value
4.3e-20
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.823
Structure
Pocket

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
  • GO:0051989 Catalysis of the reaction: coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine.
  • GO:0004109 Catalysis of the reaction: coproporphyrinogen III + 2 H+ + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX.
  • GO:0046872 Binding to a metal ion.
  • GO:0006779 The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
  • GO:0006782 The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records
Show feature table
Start End DB Term Name
63 255 CDD cd01335 Radical_SAM
14 448 PANTHER PTHR13932 COPROPORPHYRINIGEN III OXIDASE
14 448 InterPro IPR034505 Anaerobic coproporphyrinogen-III oxidase
53 276 SMART SM00729 MiaB
53 276 InterPro IPR006638 Elp3/MiaA/NifB-like, radical SAM core domain
61 284 Gene3D G3DSA:3.80.30.20 tm_1862 like domain
61 284 InterPro IPR023404 Radical SAM, alpha/beta horseshoe
3 460 SFLD SFLDG01065 anaerobic coproporphyrinogen-III oxidase like
63 254 SFLD SFLDG01082 B12-binding domain containing
368 460 FunFam G3DSA:1.10.10.920:FF:000002 Coproporphyrinogen-III oxidase
5 448 SUPERFAMILY SSF102114 Radical SAM enzymes
3 459 PIRSF PIRSF000167 HemN
3 459 InterPro IPR004558 Oxygen-independent coproporphyrinogen III oxidase HemN
6 460 NCBIfam TIGR00538 oxygen-independent coproporphyrinogen III oxidase
6 460 InterPro IPR004558 Oxygen-independent coproporphyrinogen III oxidase HemN
3 460 SFLD SFLDF00277 oxygen-independent coproporphyrinogen-III oxidase 1 (HemN-like)
3 460 InterPro IPR004558 Oxygen-independent coproporphyrinogen III oxidase HemN
58 232 Pfam PF04055 Radical SAM superfamily
58 232 InterPro IPR007197 Radical SAM
368 460 Gene3D G3DSA:1.10.10.920 -
48 287 ProSiteProfiles PS51918 Radical SAM core domain profile.
48 287 InterPro IPR007197 Radical SAM
369 435 Pfam PF06969 HemN C-terminal domain
369 435 InterPro IPR010723 HemN, C-terminal

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA1546
AlphaFold full sequence Viewing
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
1 0.616
2 0.502